Searching in Thiohalomonas denitrificans HLD2 (GCF_900102855.1)
Found 8 curated entries in PaperBLAST's database that match '6.3.1.1' as complete word(s).
These curated entries have 5 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Thiohalomonas denitrificans HLD2, or try another query
| BLP65_RS06795 SAMN03097708_01374 WP_092994459.1: N-acetylglutaminylglutamine amidotransferase is similar to: | PaperBLAST |
AsnB / b0674: asparagine synthetase B (EC 6.3.5.4; EC 6.3.1.1; EC 3.5.1.38; EC 3.5.1.2) from Escherichia coli | 30% id, 65% cov |
AsnB / b0674: asparagine synthetase B (EC 6.3.5.4; EC 6.3.1.1; EC 3.5.1.38; EC 3.5.1.2) from Escherichia coli | 37% id, 30% cov |
AsnB / b0674: asparagine synthetase B (EC 6.3.5.4; EC 6.3.1.1; EC 3.5.1.38; EC 3.5.1.2) from Escherichia coli | 33% id, 16% cov |
| asnB BLP65_RS06145 SAMN03097708_01238 WP_092994041.1: asparagine synthase (glutamine-hydrolyzing) is similar to: | PaperBLAST |
AsnB / b0674: asparagine synthetase B (EC 6.3.5.4; EC 6.3.1.1; EC 3.5.1.38; EC 3.5.1.2) from Escherichia coli | 40% id, 30% cov |
AsnB / b0674: asparagine synthetase B (EC 6.3.5.4; EC 6.3.1.1; EC 3.5.1.38; EC 3.5.1.2) from Escherichia coli | 34% id, 35% cov |
| lysS BLP65_RS06330 SAMN03097708_01275 WP_092994130.1: lysine--tRNA ligase is similar to: | PaperBLAST |
Q9V228: asparagine-tRNA ligase (EC 6.1.1.22); aspartate-ammonia ligase (EC 6.3.1.1) from Pyrococcus abyssi | 31% id, 26% cov |
| BLP65_RS05110 SAMN03097708_01030 WP_092993470.1: asparagine synthase-related protein is similar to: | PaperBLAST |
AsnB / b0674: asparagine synthetase B (EC 6.3.5.4; EC 6.3.1.1; EC 3.5.1.38; EC 3.5.1.2) from Escherichia coli | 31% id, 12% cov |
| BLP65_RS12215 SAMN03097708_02473 WP_092997548.1: ankyrin repeat domain-containing protein is similar to: | PaperBLAST |
TC 1.A.4.6.1 / Q8BLA8: Cold-activated cation channel in nociceptive sensory neurons, ANKTM1, with lower activation temperature (in the noxious cold range) than TRPM8 (TC #1.A.4.5.7) (Story et al., 2003). Also called TRPA1 (Acc #AAS78661) which translates sound into electric signals in the ear. It sits at the tips of cilia in the inner ear and allows passage of K+ and Ca2+ into the cell. Vibrations in the hair cause the channel to open and close. The frequency of the sound waves generate an electrical signal of the same frequency (Jordt et al., 2004). (Shows 25% identity with α-latrotoxin precursor (TC #1.C.6.3.1.1) in its N-terminal half.) TRPA1 is a polyunsaturated fatty acid sensor in mammals, but not in flies and fish (Motter and Ahern, 2012). TRPA1 is regulated by its N-terminal ankyrin repeat domain from Mus musculus | 29% id, 10% cov |
The hits are sorted by %identity * %coverage (highest first)
Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.
Found hits to 4 reading frames. Except for 1 reading frames, these were redundant with annotated proteins. These remaining reading frames may be pseudogenes, omissions in the genome annotation, or N-terminal extensions of annotated proteins.
| 163328-164293 (frame -3) on NZ_FMWD01000007.1 Thiohalomonas denitrificans strain HLD2, whole genome shotgun sequence is similar to: | PaperBLAST |
TC 1.A.4.6.1 / Q8BLA8: Cold-activated cation channel in nociceptive sensory neurons, ANKTM1, with lower activation temperature (in the noxious cold range) than TRPM8 (TC #1.A.4.5.7) (Story et al., 2003). Also called TRPA1 (Acc #AAS78661) which translates sound into electric signals in the ear. It sits at the tips of cilia in the inner ear and allows passage of K+ and Ca2+ into the cell. Vibrations in the hair cause the channel to open and close. The frequency of the sound waves generate an electrical signal of the same frequency (Jordt et al., 2004). (Shows 25% identity with α-latrotoxin precursor (TC #1.C.6.3.1.1) in its N-terminal half.) TRPA1 is a polyunsaturated fatty acid sensor in mammals, but not in flies and fish (Motter and Ahern, 2012). TRPA1 is regulated by its N-terminal ankyrin repeat domain from Mus musculus | 30% id, 25% cov |
Lawrence Berkeley National Laboratory